We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1z5o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1z5o.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1z5o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1z5o| PDB=1z5o | SCENE= }}
{{STRUCTURE_1z5o| PDB=1z5o | SCENE= }}
-
'''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine'''
+
===Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine===
-
==Overview==
+
<!--
-
MTA/AdoHcy nucleosidase (MTAN) irreversibly hydrolyzes the N9-C1' bond in the nucleosides, 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (AdoHcy) to form adenine and the corresponding thioribose. MTAN plays a vital role in metabolic pathways involving methionine recycling, biological methylation, polyamine biosynthesis, and quorum sensing. Crystal structures of a wild-type (WT) MTAN complexed with glycerol, and mutant-enzyme and mutant-product complexes have been determined at 2.0A, 2.0A, and 2.1A resolution, respectively. The WT MTAN-glycerol structure provides a purine-free model and in combination with the previously solved thioribose-free MTAN-ADE structure, we now have separate apo structures for both MTAN binding subsites. The purine and thioribose-free states reveal an extensive enzyme-immobilized water network in their respective binding subsites. The Asp197Asn MTAN-MTA and Glu12Gln MTAN-MTR.ADE structures are the first enzyme-substrate and enzyme-product complexes reported for MTAN, respectively. These structures provide representative snapshots along the reaction coordinate and allow insight into the conformational changes of the enzyme and the nucleoside substrate. A "catalytic movie" detailing substrate binding, catalysis, and product release is presented.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16109423}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16109423 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16109423}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Smith, G D.]]
[[Category: Smith, G D.]]
[[Category: Mixed alpha/beta]]
[[Category: Mixed alpha/beta]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:12:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:56:18 2008''

Revision as of 09:56, 29 July 2008

Image:1z5o.png

Template:STRUCTURE 1z5o

Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine

Template:ABSTRACT PUBMED 16109423

About this Structure

1Z5O is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis., Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL, J Mol Biol. 2005 Sep 23;352(3):559-74. PMID:16109423

Page seeded by OCA on Tue Jul 29 12:56:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z5o"
Personal tools